Comparative interaction of alpha-helical and beta-sheet amphiphilic isopeptides with phospholipid monolayers

Biopolymers
Régine Maget-Dana, Dominique Lelièvre

Abstract

The two sequential amphiphilic peptide isomers, (Leu-Lys-Lys-Leu)4 and (Leu-Lys)8, were chosen as models for alpha-helical and beta-sheet peptides, respectively. In order to evaluate the contribution of the secondary structure of a peptide to its penetration into cellular membranes, interactions of these isopeptides with L-alpha-dimyristoyl phosphatidylcholine (DMPC) monolayers were studied. Both isopeptides penetrate into DMPC monolayers up to an exclusion pressure of approximately 27 mN/m, but a discontinuity is observed in the penetration profile of the alpha-helical (LKKL)4. The main parameters extracted from the compression isotherms of the mixed peptide/DMPC monolayers-namely, transition pressure, mean area, elasticity modulus, and energy of mixing-were analyzed. These analyses indicate that the alpha-helical isomer interacts strongly with DMPC by forming a 1:32 (LKKL)4-DMPC complex. When engaged in this complex, (LKKL)(4) behaves as an hydrophobic helix and has a tendency to become vertically oriented in the course of the compression process. The beta-sheet (LK)8 interacts more weakly with DMPC and no complex can be detected.

References

Jan 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·B L KaganR I Lehrer
Aug 18, 1981·Biochemistry·P BougisR Verger
Jan 14, 1994·Biochemical and Biophysical Research Communications·I Z Zubrzycki, G Gäde
Nov 13, 1998·Proceedings of the National Academy of Sciences of the United States of America·S B Prusiner
Apr 9, 1999·The Journal of Peptide Research : Official Journal of the American Peptide Society·T NittoliS M Sieburth

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Citations

Jun 27, 2019·Langmuir : the ACS Journal of Surfaces and Colloids·Joanna Juhaniewicz-DębińskaSławomir Sęk
Dec 28, 2005·Langmuir : the ACS Journal of Surfaces and Colloids·Jorge CasasConcepción Mestres

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